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Reviewed, UniProtKB/Swiss-Prot P0ABR9 (MHPB_ECOLI)

Last modified June 15, 2010. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
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Names and originHide

Protein namesRecommended name:
2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase

EC=1.13.11.16
Gene names
Name:mhpB
Ordered Locus Names:b0348, JW0339
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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Protein attributesHide

Sequence length314 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.
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General annotation (Comments)Hide

Function

Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively. Ref.6

Catalytic activity

3-(2,3-dihydroxyphenyl)propanoate + O2 = 2-hydroxy-6-oxonona-2,4-diene-1,9-dioate. HAMAP MF_01653

2,3-dihydroxicinnamic acid + O2 = 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate. HAMAP MF_01653

Pathway

Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP MF_01653

Subunit structure

Homotetramer. Ref.6

Sequence similarities

Belongs to the ligB/mhpB extradiol dioxygenase family.

Biophysicochemical properties

Kinetic parameters:

KM=26 µM for 2,3-dihydroxyphenylpropionic acid (at 20 degrees Celsius and pH 8) HAMAP MF_01653

KM=36 µM for 2,3-dihydroxycinnamic acid (at 20 degrees Celsius and pH 8)

KM=37 µM for methyl-2,3-dihydroxyphenylpropionate (at 20 degrees Celsius and pH 8)

KM=90 µM for 3-methylcatechol (at 20 degrees Celsius and pH 8)

KM=94 µM for 3-phenethylcatechol (at 20 degrees Celsius and pH 8)

KM=154 µM for 3-propylcatechol (at 20 degrees Celsius and pH 8)

KM=185 µM for 3-ethylcatechol (at 20 degrees Celsius and pH 8)

KM=300 µM for 2,3-dihydroxyphenoxyacetic acid (at 20 degrees Celsius and pH 8)

KM=700 µM for catechol (at 20 degrees Celsius and pH 8)

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Sequence annotation (Features)Hide

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3143142,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase HAMAP MF_01653
PRO_0000085103

Sites

Active site1151Proton donor HAMAP MF_01653
Active site1791Proton acceptor HAMAP MF_01653

Experimental info

Mutagenesis1141D → A: Complete loss of extradiol cleavage activity. Ref.7
Mutagenesis1141D → N: Low level of catalytic activity, 600-fold lower than the wild-type enzyme. More than 8000-fold decrease in affinity. Ref.7
Mutagenesis1151H → A: Complete loss of extradiol cleavage activity. Ref.7
Mutagenesis1151H → Q: Complete loss of activity. Ref.7
Mutagenesis1151H → Y: Complete loss of activity. Ref.7
Mutagenesis1791H → A: Complete loss of activity. Ref.7
Mutagenesis1791H → Q: Complete loss of activity. Ref.7
Mutagenesis1791H → Y: Complete loss of activity. Ref.7
Mutagenesis1811P → A: More than 2-fold decrease in catalytic activity and 100-fold decrease in affinity. Ref.7
Mutagenesis1811P → H: More than 60-fold decrease in catalytic activity and affinity. Ref.7
Sequence conflict138 – 1403ING → NKA in BAA13053. Ref.1
Sequence conflict1521R → H in BAA13053. Ref.1
Sequence conflict1571A → T in BAA13053. Ref.1
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SequencesHide

Sequence LengthMass (Da)Tools
P0ABR9-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: E1D5A8574E5DFE05

FASTA31434,196
        10         20         30         40         50         60 
MHAYLHCLSH SPLVGYVDPA QEVLDEVNGV IASARERIAA FSPELVVLFA PDHYNGFFYD 

        70         80         90        100        110        120 
VMPPFCLGVG ATAIGDFGSA AGELPVPVEL AEACAHAVMK SGIDLAVSYC MQVDHGFAQP 

       130        140        150        160        170        180 
LEFLLGGLDK VPVLPVFING VATPLPGFQR TRMLGEAIGR FTSTLNKRVL FLGSGGLSHQ 

       190        200        210        220        230        240 
PPVPELAKAD AHMRDRLLGS GKDLPASERE LRQQRVISAA EKFVEDQRTL HPLNPIWDNQ 

       250        260        270        280        290        300 
FMTLLEQGRI QELDAVSNEE LSAIAGKSTH EIKTWVAAFA AISAFGNWRS EGRYYRPIPE 

       310 
WIAGFGSLSA RTEN 

« Hide

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ReferencesHide

« Hide 'large scale' references
[1]"Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): sequence analysis and biochemical properties of a third family of extradiol dioxygenases."
Spence E.L., Kawamukai M., Sanvoisin J., Braven H., Bugg T.D.H.
J. Bacteriol. 178:5249-5256(1996) [PubMed: 8752345] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], BIOPHYSICOCHEMICAL PROPERTIES.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12."
Ferrandez A., Garcia J.L., Diaz E.
J. Bacteriol. 179:2573-2581(1997) [PubMed: 9098055] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / CS520.
[3]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Overproduction, purification and properties of 2,3-dihydroxyphenylpropionate 1,2-dioxygenase from Escherichia coli."
Bugg T.D.H.
Biochim. Biophys. Acta 1202:258-264(1993) [PubMed: 8399388] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-15, SUBUNIT, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
[7]"Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: site-directed mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB)."
Mendel S., Arndt A., Bugg T.D.H.
Biochemistry 43:13390-13396(2004) [PubMed: 15491145] [Abstract]
Cited for: MUTAGENESIS OF ASP-114; HIS-115; HIS-179 AND PRO-181, REACTION MECHANISM.
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Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ
D86239 Genomic DNA. Translation: BAA13053.1.
Y09555 Genomic DNA. Translation: CAA70748.1.
U73857 Genomic DNA. Translation: AAB18072.1.
U00096 Genomic DNA. Translation: AAC73451.1.
AP009048 Genomic DNA. Translation: BAE76130.1.
PIRD64762.
RefSeqAP_001000.1.
NP_414882.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP0ABR9.

Genome annotation databases

EnsemblBacteriaEBESCT00000003464; EBESCP00000003464; EBESCG00000002840.
EBESCT00000017975; EBESCP00000017266; EBESCG00000017031.
GeneID945047.
GenomeReviewsGene locus JW0339 in contig AP009048_GR.
Gene locus b0348 in contig U00096_GR.
KEGGecj:JW0339.
eco:b0348.

Organism-specific databases

EchoBASEEB4167.
EcoGeneEG20274. mhpB.
CMRSearch...

Phylogenomic databases

eggNOGNOG42398.
HOGENOMHBG565586.
OMAPLNPEWD.
ProtClustDBPRK13370.

Enzyme and pathway databases

BioCycEcoCyc:DHPDIOXYGEN-MONOMER.
ECOL168927:B0348-MONOMER.
MetaCyc:DHPDIOXYGEN-MONOMER.
BRENDA1.13.11.16. 246.

Gene expression databases

GenevestigatorP0ABR9.

Family and domain databases

HAMAPMF_01653. MhpB.
[Tree]
InterProIPR004183. Xdiol_dOase_3B.
[Graphical view]
PfamPF02900. LigB. 1 hit.
[Graphical view]
SUPFAMSSF53213. Xdiol_dOase_3B. 1 hit.
ProtoNetSearch...
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Entry informationHide

Entry nameMHPB_ECOLI
AccessionPrimary (citable) accession number: P0ABR9
Secondary accession number(s): P54711 expand/collapse secondary AC list , P77048, P77461, Q2MC76
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: June 15, 2010
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
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Relevant documentsHide

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents